GenomeNet

Database: UniProt/TrEMBL
Entry: A0A1I7V5E5_LOALO
LinkDB: A0A1I7V5E5_LOALO
Original site: A0A1I7V5E5_LOALO 
ID   A0A1I7V5E5_LOALO        Unreviewed;      1028 AA.
AC   A0A1I7V5E5; A0A1S0TUT3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   28-FEB-2018, entry version 9.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
GN   ORFNames=LOAG_08740 {ECO:0000313|EMBL:EFO19754.1,
GN   ECO:0000313|WBParaSite:EN70_10068};
OS   Loa loa (Eye worm) (Filaria loa).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Spirurida;
OC   Spiruromorpha; Filarioidea; Onchocercidae; Loa.
OX   NCBI_TaxID=7209 {ECO:0000313|Proteomes:UP000095285, ECO:0000313|WBParaSite:EN70_10068};
RN   [1] {ECO:0000313|EMBL:EFO19754.1}
RP   NUCLEOTIDE SEQUENCE.
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA   Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., White J.,
RA   Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Loa loa.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000095285, ECO:0000313|WBParaSite:EN70_10068}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25217238; DOI=10.1186/1471-2164-15-788;
RA   Tallon L.J., Liu X., Bennuru S., Chibucos M.C., Godinez A., Ott S.,
RA   Zhao X., Sadzewicz L., Fraser C.M., Nutman T.B., Dunning Hotopp J.C.;
RT   "Single molecule sequencing and genome assembly of a clinical specimen
RT   of Loa loa, the causative agent of loiasis.";
RL   BMC Genomics 15:788-788(2014).
RN   [3] {ECO:0000313|WBParaSite:EN70_10068}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361144};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU361144};
CC   -!- SIMILARITY: Belongs to the peptidase M2 family.
CC       {ECO:0000256|RuleBase:RU361144}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; JH712109; EFO19754.1; -; Genomic_DNA.
DR   RefSeq; XP_003144317.1; XM_003144269.1.
DR   GeneID; 9946166; -.
DR   KEGG; loa:LOAG_08740; -.
DR   WBParaSite; EN70_10068; EN70_10068; EN70_10068.
DR   CTD; 9946166; -.
DR   KO; K01283; -.
DR   OMA; REVQENF; -.
DR   Proteomes; UP000095285; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro.
DR   CDD; cd06461; M2_ACE; 1.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; PTHR10514; 1.
DR   Pfam; PF01401; Peptidase_M2; 1.
DR   PRINTS; PR00791; PEPDIPTASEA.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|RuleBase:RU361144};
KW   Complete proteome {ECO:0000313|Proteomes:UP000095285};
KW   Glycoprotein {ECO:0000256|RuleBase:RU361144};
KW   Hydrolase {ECO:0000256|RuleBase:RU361144};
KW   Metal-binding {ECO:0000256|RuleBase:RU361144};
KW   Metalloprotease {ECO:0000256|RuleBase:RU361144};
KW   Protease {ECO:0000256|RuleBase:RU361144};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095285};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU361144}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23   1028       Angiotensin-converting enzyme.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5010173271.
SQ   SEQUENCE   1028 AA;  115645 MW;  BD789A80F159197D CRC64;
     MIRRTLLLQQ LIISVVLLRL HAQHEDNSSG QNGSRKDTGI STLESSLTLS RNSAIWPTLM
     QSTVNDAPII AAAEAKNILR TYSIAKQPTP LSKLSSQNHS TEFSAQPNSK PEPEQEIVSS
     SSFHPTISKS GFHHQPILTT TAKFAKPFAD GSSHLAMHSA QVPQLTVHGE DPQPLPEPNA
     VKVSGASLMP SYQNNAFEDD TEQFDDEDDS SADSSRPGAI DNEAIEELVN RFLNGDDTED
     GKEEKLNKEA LKLINSSKYW DLNNLQPENS IRDSKKAQEW MNGYAVEAQK VLREVALAGW
     NYVTSVSHLT KQLLDEAEET LGKFVKSTSK QAKQFDTKAI EDESLKRQFE LLLVEGINVL
     DENDFNEYNE LQKLIAKAYA ETSVCETSNA TICPYRVSDI VSIIAHENDG PKAFRFWIAL
     REALGPKLVT SYKRLIELIN KGAKLNGFPD GGAMWRSPYE RFASRREKTE QSDTVALLQK
     LYQQINPFYK QLHAYIRRQI PALYGLANVS NLTRDGPIPA HLLKSIASDN WVAFYRDTKP
     YQDEDHLARE VQENFQKLNY TVKNMFKQTY KTLKQLGFDK LPSSFWTKSI FTRTWSKDML
     CHPPAAYDMR DKHDYRIKAC AHLNLPDFEL THKLLVHIYH YYMCRDQPLL FREATNPSLL
     TAVTNAFAIN ARNIEYLKMM KLITSETGFS HSKIINRLYL EALEDFVKLP FDFAVDMWRF
     HIFDGTSTNA TWNSDWWQLS ELFQGIKSPV ERKSTDFDAI AFSTIAQTHA PAMKHFFAYI
     MQFQILKALC PDTTNLSNGC MLERNSVIDK IKKVMALGSS ITWREALEII TGSKEVDASA
     MLEYYQPLIS WLEEQNAKEH AYIGWDGFGK PFEESEVPKV RESTTSTDSL SEILSGSQFA
     FPGGDCSNGK ECLLDSVCQN DLCECKEGLY TLKIGNTYNC VPGNPADAGF GDGHGGLVIG
     LHSIDDNSIV AIPEPEEHEK QMKAEPEPEL ANDKPGFLPE QELKSKGTSA SIPTLTLVLS
     LTVLVVLL
//
DBGET integrated database retrieval system